HEADER CHAPERONE 29-NOV-06 2O1U
TITLE STRUCTURE OF FULL LENGTH GRP94 WITH AMP-PNP BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPLASMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 73-754;
COMPND 5 SYNONYM: HEAT SHOCK PROTEIN 90 KDA BETA MEMBER 1, 94 KDA GLUCOSE-
COMPND 6 REGULATED PROTEIN, GRP94;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 STRAIN: FAMILIARIS;
SOURCE 6 GENE: HSP90B1, TRA1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B-GRP94(73-754D41)
KEYWDS GRP94, HSP82, HSP90, HTPG, CHAPERONE, AMP-PNP, GP96, ENDOPLASMIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.DOLLINS,J.J.WARREN,R.M.IMMORMINO,D.T.GEWIRTH
REVDAT 6 03-APR-24 2O1U 1 REMARK
REVDAT 5 27-DEC-23 2O1U 1 SEQADV LINK
REVDAT 4 02-AUG-17 2O1U 1 SOURCE
REVDAT 3 13-JUL-11 2O1U 1 VERSN
REVDAT 2 24-FEB-09 2O1U 1 VERSN
REVDAT 1 23-OCT-07 2O1U 0
JRNL AUTH D.E.DOLLINS,J.J.WARREN,R.M.IMMORMINO,D.T.GEWIRTH
JRNL TITL STRUCTURES OF GRP94-NUCLEOTIDE COMPLEXES REVEAL MECHANISTIC
JRNL TITL 2 DIFFERENCES BETWEEN THE HSP90 CHAPERONES.
JRNL REF MOL.CELL V. 28 41 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17936703
JRNL DOI 10.1016/J.MOLCEL.2007.08.024
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 60745
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3196
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4443
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 238
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.67000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : -1.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.387
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.280
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.611
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9497 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12834 ; 1.335 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1148 ; 2.506 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 437 ;25.613 ;24.485
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1748 ;10.332 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;13.440 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1438 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7013 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4229 ; 0.171 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6541 ; 0.309 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 630 ; 0.179 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.201 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 42 ; 0.150 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.164 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5973 ; 0.484 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9289 ; 0.860 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4072 ; 0.957 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3543 ; 1.509 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 85 A 749 6
REMARK 3 1 B 87 B 749 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 4450 ; 0.76 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 4450 ; 1.58 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 85 A 749
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5792 34.7777 26.2872
REMARK 3 T TENSOR
REMARK 3 T11: 0.0244 T22: -0.3795
REMARK 3 T33: -0.3451 T12: 0.1048
REMARK 3 T13: 0.0595 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 0.7853 L22: 1.3915
REMARK 3 L33: 5.0596 L12: 0.0442
REMARK 3 L13: 0.3193 L23: 0.4302
REMARK 3 S TENSOR
REMARK 3 S11: -0.0481 S12: -0.1878 S13: -0.0433
REMARK 3 S21: 0.6288 S22: 0.1675 S23: 0.0709
REMARK 3 S31: 0.4111 S32: -0.1774 S33: -0.1194
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 749
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7131 24.0729 28.5541
REMARK 3 T TENSOR
REMARK 3 T11: -0.1906 T22: -0.3065
REMARK 3 T33: -0.2246 T12: 0.0054
REMARK 3 T13: -0.1457 T23: 0.0598
REMARK 3 L TENSOR
REMARK 3 L11: 0.6766 L22: 1.5944
REMARK 3 L33: 5.3781 L12: 0.3155
REMARK 3 L13: -0.4845 L23: 0.4587
REMARK 3 S TENSOR
REMARK 3 S11: 0.0889 S12: -0.1613 S13: 0.1311
REMARK 3 S21: 0.5094 S22: 0.0630 S23: -0.2773
REMARK 3 S31: -0.1399 S32: 0.2725 S33: -0.1519
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2O1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 47.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: GRP94(73-754D41)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-32% V/V PEG400, 150-225MM MGCL2,
REMARK 280 AND 0.1M BIS-TRIS PROPANE, PH 6.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 49.66500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.44350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.63000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.44350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.66500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.63000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: DIMER IN ASYMMETRIC UNIT REPRESENTS THE BIOLOGICAL DIMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 52
REMARK 465 GLY A 53
REMARK 465 SER A 54
REMARK 465 SER A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 HIS A 60
REMARK 465 HIS A 61
REMARK 465 SER A 62
REMARK 465 SER A 63
REMARK 465 GLY A 64
REMARK 465 LEU A 65
REMARK 465 VAL A 66
REMARK 465 PRO A 67
REMARK 465 ARG A 68
REMARK 465 GLY A 69
REMARK 465 SER A 70
REMARK 465 HIS A 71
REMARK 465 MET A 72
REMARK 465 SER A 73
REMARK 465 GLU A 74
REMARK 465 LYS A 75
REMARK 465 PHE A 76
REMARK 465 ALA A 77
REMARK 465 PHE A 78
REMARK 465 GLN A 79
REMARK 465 ALA A 80
REMARK 465 GLU A 81
REMARK 465 VAL A 82
REMARK 465 ASN A 83
REMARK 465 ARG A 84
REMARK 465 ILE A 166
REMARK 465 ALA A 167
REMARK 465 LYS A 168
REMARK 465 SER A 169
REMARK 465 GLY A 170
REMARK 465 THR A 171
REMARK 465 SER A 172
REMARK 465 GLU A 173
REMARK 465 PHE A 174
REMARK 465 LEU A 175
REMARK 465 ASN A 176
REMARK 465 LYS A 177
REMARK 465 MET A 178
REMARK 465 THR A 179
REMARK 465 GLU A 180
REMARK 465 ALA A 181
REMARK 465 GLN A 182
REMARK 465 GLU A 183
REMARK 465 ASP A 184
REMARK 465 GLY A 185
REMARK 465 GLN A 186
REMARK 465 SER A 187
REMARK 465 THR A 188
REMARK 465 SER A 189
REMARK 465 GLU A 190
REMARK 465 LEU A 191
REMARK 465 ILE A 192
REMARK 465 GLY A 193
REMARK 465 GLN A 194
REMARK 465 PHE A 195
REMARK 465 GLY A 196
REMARK 465 THR A 286
REMARK 465 GLY A 287
REMARK 465 GLY A 288
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 LYS A 328
REMARK 465 THR A 329
REMARK 465 GLY A 396
REMARK 465 LEU A 397
REMARK 465 PHE A 398
REMARK 465 ASP A 399
REMARK 465 GLU A 400
REMARK 465 TYR A 401
REMARK 465 GLY A 402
REMARK 465 SER A 403
REMARK 465 LYS A 404
REMARK 465 LYS A 405
REMARK 465 SER A 406
REMARK 465 ASP A 407
REMARK 465 ASP A 750
REMARK 465 PRO A 751
REMARK 465 ASP A 752
REMARK 465 ALA A 753
REMARK 465 LYS A 754
REMARK 465 MET B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 SER B 55
REMARK 465 HIS B 56
REMARK 465 HIS B 57
REMARK 465 HIS B 58
REMARK 465 HIS B 59
REMARK 465 HIS B 60
REMARK 465 HIS B 61
REMARK 465 SER B 62
REMARK 465 SER B 63
REMARK 465 GLY B 64
REMARK 465 LEU B 65
REMARK 465 VAL B 66
REMARK 465 PRO B 67
REMARK 465 ARG B 68
REMARK 465 GLY B 69
REMARK 465 SER B 70
REMARK 465 HIS B 71
REMARK 465 MET B 72
REMARK 465 SER B 73
REMARK 465 GLU B 74
REMARK 465 LYS B 75
REMARK 465 PHE B 76
REMARK 465 ALA B 77
REMARK 465 PHE B 78
REMARK 465 GLN B 79
REMARK 465 ALA B 80
REMARK 465 GLU B 81
REMARK 465 VAL B 82
REMARK 465 ASN B 83
REMARK 465 ARG B 84
REMARK 465 MET B 85
REMARK 465 MET B 86
REMARK 465 ILE B 166
REMARK 465 ALA B 167
REMARK 465 LYS B 168
REMARK 465 SER B 169
REMARK 465 GLY B 170
REMARK 465 THR B 171
REMARK 465 SER B 172
REMARK 465 GLU B 173
REMARK 465 PHE B 174
REMARK 465 LEU B 175
REMARK 465 ASN B 176
REMARK 465 LYS B 177
REMARK 465 MET B 178
REMARK 465 THR B 179
REMARK 465 GLU B 180
REMARK 465 ALA B 181
REMARK 465 GLN B 182
REMARK 465 GLU B 183
REMARK 465 ASP B 184
REMARK 465 GLY B 185
REMARK 465 GLN B 186
REMARK 465 SER B 187
REMARK 465 THR B 188
REMARK 465 SER B 189
REMARK 465 GLU B 190
REMARK 465 LEU B 191
REMARK 465 ILE B 192
REMARK 465 GLY B 193
REMARK 465 GLN B 194
REMARK 465 PHE B 195
REMARK 465 GLY B 196
REMARK 465 GLY B 287
REMARK 465 GLY B 288
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 465 LYS B 328
REMARK 465 THR B 329
REMARK 465 PRO B 394
REMARK 465 ARG B 395
REMARK 465 GLY B 396
REMARK 465 LEU B 397
REMARK 465 PHE B 398
REMARK 465 ASP B 399
REMARK 465 GLU B 400
REMARK 465 TYR B 401
REMARK 465 GLY B 402
REMARK 465 SER B 403
REMARK 465 LYS B 404
REMARK 465 LYS B 405
REMARK 465 SER B 406
REMARK 465 ASP B 407
REMARK 465 ASP B 750
REMARK 465 PRO B 751
REMARK 465 ASP B 752
REMARK 465 ALA B 753
REMARK 465 LYS B 754
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 85 CG SD CE
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 LYS A 364 CG CD CE NZ
REMARK 470 ARG A 395 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 446 CG1 CG2
REMARK 470 GLU A 449 CG CD OE1 OE2
REMARK 470 LYS A 455 CG CD CE NZ
REMARK 470 LYS A 463 CG CD CE NZ
REMARK 470 ARG A 466 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 582 CG CD OE1 OE2
REMARK 470 ARG A 587 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 603 CG CD CE NZ
REMARK 470 GLN A 668 CG CD OE1 NE2
REMARK 470 THR A 669 OG1 CG2
REMARK 470 LYS A 671 CG CD CE NZ
REMARK 470 ASP A 672 CG OD1 OD2
REMARK 470 ILE A 673 CG1 CG2 CD1
REMARK 470 SER A 674 OG
REMARK 470 THR A 675 OG1 CG2
REMARK 470 ASN A 676 CG OD1 ND2
REMARK 470 TYR A 677 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 747 CG CD1 CD2
REMARK 470 ASN A 748 CG OD1 ND2
REMARK 470 ILE A 749 CG1 CG2 CD1
REMARK 470 TYR B 94 N
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 LYS B 364 CG CD CE NZ
REMARK 470 GLU B 365 CG CD OE1 OE2
REMARK 470 LYS B 434 CG CD CE NZ
REMARK 470 VAL B 446 CG1 CG2
REMARK 470 GLU B 449 CG CD OE1 OE2
REMARK 470 LYS B 455 CG CD CE NZ
REMARK 470 LYS B 462 CG CD CE NZ
REMARK 470 LYS B 486 CG CD CE NZ
REMARK 470 LYS B 534 CG CD CE NZ
REMARK 470 LYS B 603 CG CD CE NZ
REMARK 470 LYS B 605 CG CD CE NZ
REMARK 470 ASP B 624 CG OD1 OD2
REMARK 470 GLN B 651 CG CD OE1 NE2
REMARK 470 LYS B 663 CG CD CE NZ
REMARK 470 LYS B 671 CG CD CE NZ
REMARK 470 ASP B 672 CG OD1 OD2
REMARK 470 ILE B 673 CG1 CG2 CD1
REMARK 470 SER B 674 OG
REMARK 470 ASN B 676 CG OD1 ND2
REMARK 470 TYR B 677 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 748 CG OD1 ND2
REMARK 470 ILE B 749 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 451 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 86 -72.03 -77.86
REMARK 500 LYS A 95 -72.37 -75.35
REMARK 500 ASP A 139 67.00 -111.01
REMARK 500 ASN A 143 42.37 71.96
REMARK 500 LYS A 161 -62.65 -102.14
REMARK 500 LEU A 163 71.00 -102.11
REMARK 500 ASN A 217 45.16 -102.09
REMARK 500 ASP A 218 166.99 170.03
REMARK 500 SER A 227 -28.87 156.53
REMARK 500 ASN A 228 -92.52 -98.39
REMARK 500 ASP A 257 -12.75 -157.84
REMARK 500 LEU A 259 45.37 -74.39
REMARK 500 ASP A 262 -21.64 -147.08
REMARK 500 SER A 363 -6.51 -148.36
REMARK 500 LYS A 364 -135.93 59.25
REMARK 500 GLU A 365 -16.93 74.44
REMARK 500 SER A 519 -34.67 -137.59
REMARK 500 LYS A 625 -64.87 -139.61
REMARK 500 LYS A 630 -37.22 -140.60
REMARK 500 THR A 641 -75.02 -121.57
REMARK 500 THR A 669 -49.64 -139.47
REMARK 500 LYS A 671 56.14 -112.01
REMARK 500 ASP A 672 77.40 57.02
REMARK 500 ASN A 676 -110.19 -78.69
REMARK 500 TYR A 677 -69.18 -147.59
REMARK 500 TYR A 678 57.21 -109.74
REMARK 500 ALA A 679 -45.38 -132.18
REMARK 500 SER A 680 35.16 -99.73
REMARK 500 ASP A 731 98.39 -166.17
REMARK 500 LEU A 747 -87.11 -151.86
REMARK 500 ASN A 748 -29.87 -176.46
REMARK 500 LEU B 88 16.95 -140.20
REMARK 500 SER B 92 -40.21 -146.95
REMARK 500 LEU B 126 48.16 -88.49
REMARK 500 LYS B 208 109.40 -166.82
REMARK 500 ASP B 226 49.59 -100.94
REMARK 500 SER B 227 -18.08 65.15
REMARK 500 ASN B 276 39.02 -98.24
REMARK 500 SER B 366 -45.45 76.51
REMARK 500 ASP B 420 13.59 -140.93
REMARK 500 ASN B 445 43.08 -80.64
REMARK 500 THR B 483 -60.54 -107.06
REMARK 500 SER B 519 -36.47 -131.33
REMARK 500 LYS B 625 -73.52 -117.28
REMARK 500 THR B 641 -65.56 -128.82
REMARK 500 ARG B 660 -74.09 -61.13
REMARK 500 GLN B 665 -13.71 -153.17
REMARK 500 LYS B 671 155.66 85.62
REMARK 500 SER B 680 33.58 -91.07
REMARK 500 ASP B 704 -52.22 -130.12
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 107 OD1
REMARK 620 2 ANP A 755 O1G 160.5
REMARK 620 3 ANP A 755 O1A 79.6 82.5
REMARK 620 4 ANP A 755 O2B 90.4 98.5 94.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 107 OD1
REMARK 620 2 ANP B 755 O1G 100.1
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O1V RELATED DB: PDB
REMARK 900 STRUCTURE OF FULL LENGTH GRP94 WITH ADP BOUND
REMARK 900 RELATED ID: 2O1W RELATED DB: PDB
REMARK 900 STRUCTURE OF N-TERMINAL PLUS MIDDLE DOMAINS (N+M) OF GRP94
REMARK 900 RELATED ID: 2O1T RELATED DB: PDB
REMARK 900 STRUCTURE OF MIDDLE PLUS C-TERMINAL DOMAINS (M+C) OF GRP94
REMARK 900 RELATED ID: 1TC6 RELATED DB: PDB
REMARK 900 LIGAND INDUCED CONFORMATIONAL SHIFT IN THE N-TERMINAL DOMAIN OF
REMARK 900 GRP94, OPEN CONFORMATION ADP-COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE DATABASE RESIDUES 287-327 WERE DELETED
REMARK 999 AND REPLACED BY 4 GLYCINES.
DBREF 2O1U A 73 286 UNP P41148 ENPL_CANFA 73 286
DBREF 2O1U A 328 754 UNP P41148 ENPL_CANFA 328 754
DBREF 2O1U B 73 286 UNP P41148 ENPL_CANFA 73 286
DBREF 2O1U B 328 754 UNP P41148 ENPL_CANFA 328 754
SEQADV 2O1U MET A 52 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY A 53 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER A 54 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER A 55 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 56 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 57 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 58 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 59 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 60 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 61 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER A 62 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER A 63 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY A 64 UNP P41148 EXPRESSION TAG
SEQADV 2O1U LEU A 65 UNP P41148 EXPRESSION TAG
SEQADV 2O1U VAL A 66 UNP P41148 EXPRESSION TAG
SEQADV 2O1U PRO A 67 UNP P41148 EXPRESSION TAG
SEQADV 2O1U ARG A 68 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY A 69 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER A 70 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS A 71 UNP P41148 EXPRESSION TAG
SEQADV 2O1U MET A 72 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY A 287 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY A 288 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY A 289 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY A 290 UNP P41148 SEE REMARK 999
SEQADV 2O1U MET B 52 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY B 53 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER B 54 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER B 55 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 56 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 57 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 58 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 59 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 60 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 61 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER B 62 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER B 63 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY B 64 UNP P41148 EXPRESSION TAG
SEQADV 2O1U LEU B 65 UNP P41148 EXPRESSION TAG
SEQADV 2O1U VAL B 66 UNP P41148 EXPRESSION TAG
SEQADV 2O1U PRO B 67 UNP P41148 EXPRESSION TAG
SEQADV 2O1U ARG B 68 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY B 69 UNP P41148 EXPRESSION TAG
SEQADV 2O1U SER B 70 UNP P41148 EXPRESSION TAG
SEQADV 2O1U HIS B 71 UNP P41148 EXPRESSION TAG
SEQADV 2O1U MET B 72 UNP P41148 EXPRESSION TAG
SEQADV 2O1U GLY B 287 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY B 288 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY B 289 UNP P41148 SEE REMARK 999
SEQADV 2O1U GLY B 290 UNP P41148 SEE REMARK 999
SEQRES 1 A 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 666 LEU VAL PRO ARG GLY SER HIS MET SER GLU LYS PHE ALA
SEQRES 3 A 666 PHE GLN ALA GLU VAL ASN ARG MET MET LYS LEU ILE ILE
SEQRES 4 A 666 ASN SER LEU TYR LYS ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 5 A 666 LEU ILE SER ASN ALA SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 6 A 666 LEU ILE SER LEU THR ASP GLU ASN ALA LEU ALA GLY ASN
SEQRES 7 A 666 GLU GLU LEU THR VAL LYS ILE LYS CYS ASP LYS GLU LYS
SEQRES 8 A 666 ASN LEU LEU HIS VAL THR ASP THR GLY VAL GLY MET THR
SEQRES 9 A 666 ARG GLU GLU LEU VAL LYS ASN LEU GLY THR ILE ALA LYS
SEQRES 10 A 666 SER GLY THR SER GLU PHE LEU ASN LYS MET THR GLU ALA
SEQRES 11 A 666 GLN GLU ASP GLY GLN SER THR SER GLU LEU ILE GLY GLN
SEQRES 12 A 666 PHE GLY VAL GLY PHE TYR SER ALA PHE LEU VAL ALA ASP
SEQRES 13 A 666 LYS VAL ILE VAL THR SER LYS HIS ASN ASN ASP THR GLN
SEQRES 14 A 666 HIS ILE TRP GLU SER ASP SER ASN GLU PHE SER VAL ILE
SEQRES 15 A 666 ALA ASP PRO ARG GLY ASN THR LEU GLY ARG GLY THR THR
SEQRES 16 A 666 ILE THR LEU VAL LEU LYS GLU GLU ALA SER ASP TYR LEU
SEQRES 17 A 666 GLU LEU ASP THR ILE LYS ASN LEU VAL LYS LYS TYR SER
SEQRES 18 A 666 GLN PHE ILE ASN PHE PRO ILE TYR VAL TRP SER SER LYS
SEQRES 19 A 666 THR GLY GLY GLY GLY LYS THR VAL TRP ASP TRP GLU LEU
SEQRES 20 A 666 MET ASN ASP ILE LYS PRO ILE TRP GLN ARG PRO SER LYS
SEQRES 21 A 666 GLU VAL GLU ASP ASP GLU TYR LYS ALA PHE TYR LYS SER
SEQRES 22 A 666 PHE SER LYS GLU SER ASP ASP PRO MET ALA TYR ILE HIS
SEQRES 23 A 666 PHE THR ALA GLU GLY GLU VAL THR PHE LYS SER ILE LEU
SEQRES 24 A 666 PHE VAL PRO THR SER ALA PRO ARG GLY LEU PHE ASP GLU
SEQRES 25 A 666 TYR GLY SER LYS LYS SER ASP TYR ILE LYS LEU TYR VAL
SEQRES 26 A 666 ARG ARG VAL PHE ILE THR ASP ASP PHE HIS ASP MET MET
SEQRES 27 A 666 PRO LYS TYR LEU ASN PHE VAL LYS GLY VAL VAL ASP SER
SEQRES 28 A 666 ASP ASP LEU PRO LEU ASN VAL SER ARG GLU THR LEU GLN
SEQRES 29 A 666 GLN HIS LYS LEU LEU LYS VAL ILE ARG LYS LYS LEU VAL
SEQRES 30 A 666 ARG LYS THR LEU ASP MET ILE LYS LYS ILE ALA ASP GLU
SEQRES 31 A 666 LYS TYR ASN ASP THR PHE TRP LYS GLU PHE GLY THR ASN
SEQRES 32 A 666 ILE LYS LEU GLY VAL ILE GLU ASP HIS SER ASN ARG THR
SEQRES 33 A 666 ARG LEU ALA LYS LEU LEU ARG PHE GLN SER SER HIS HIS
SEQRES 34 A 666 PRO SER ASP ILE THR SER LEU ASP GLN TYR VAL GLU ARG
SEQRES 35 A 666 MET LYS GLU LYS GLN ASP LYS ILE TYR PHE MET ALA GLY
SEQRES 36 A 666 SER SER ARG LYS GLU ALA GLU SER SER PRO PHE VAL GLU
SEQRES 37 A 666 ARG LEU LEU LYS LYS GLY TYR GLU VAL ILE TYR LEU THR
SEQRES 38 A 666 GLU PRO VAL ASP GLU TYR CYS ILE GLN ALA LEU PRO GLU
SEQRES 39 A 666 PHE ASP GLY LYS ARG PHE GLN ASN VAL ALA LYS GLU GLY
SEQRES 40 A 666 VAL LYS PHE ASP GLU SER GLU LYS THR LYS GLU SER ARG
SEQRES 41 A 666 GLU ALA ILE GLU LYS GLU PHE GLU PRO LEU LEU ASN TRP
SEQRES 42 A 666 MET LYS ASP LYS ALA LEU LYS ASP LYS ILE GLU LYS ALA
SEQRES 43 A 666 VAL VAL SER GLN ARG LEU THR GLU SER PRO CYS ALA LEU
SEQRES 44 A 666 VAL ALA SER GLN TYR GLY TRP SER GLY ASN MET GLU ARG
SEQRES 45 A 666 ILE MET LYS ALA GLN ALA TYR GLN THR GLY LYS ASP ILE
SEQRES 46 A 666 SER THR ASN TYR TYR ALA SER GLN LYS LYS THR PHE GLU
SEQRES 47 A 666 ILE ASN PRO ARG HIS PRO LEU ILE LYS ASP MET LEU ARG
SEQRES 48 A 666 ARG VAL LYS GLU ASP GLU ASP ASP LYS THR VAL SER ASP
SEQRES 49 A 666 LEU ALA VAL VAL LEU PHE GLU THR ALA THR LEU ARG SER
SEQRES 50 A 666 GLY TYR LEU LEU PRO ASP THR LYS ALA TYR GLY ASP ARG
SEQRES 51 A 666 ILE GLU ARG MET LEU ARG LEU SER LEU ASN ILE ASP PRO
SEQRES 52 A 666 ASP ALA LYS
SEQRES 1 B 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 666 LEU VAL PRO ARG GLY SER HIS MET SER GLU LYS PHE ALA
SEQRES 3 B 666 PHE GLN ALA GLU VAL ASN ARG MET MET LYS LEU ILE ILE
SEQRES 4 B 666 ASN SER LEU TYR LYS ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 5 B 666 LEU ILE SER ASN ALA SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 6 B 666 LEU ILE SER LEU THR ASP GLU ASN ALA LEU ALA GLY ASN
SEQRES 7 B 666 GLU GLU LEU THR VAL LYS ILE LYS CYS ASP LYS GLU LYS
SEQRES 8 B 666 ASN LEU LEU HIS VAL THR ASP THR GLY VAL GLY MET THR
SEQRES 9 B 666 ARG GLU GLU LEU VAL LYS ASN LEU GLY THR ILE ALA LYS
SEQRES 10 B 666 SER GLY THR SER GLU PHE LEU ASN LYS MET THR GLU ALA
SEQRES 11 B 666 GLN GLU ASP GLY GLN SER THR SER GLU LEU ILE GLY GLN
SEQRES 12 B 666 PHE GLY VAL GLY PHE TYR SER ALA PHE LEU VAL ALA ASP
SEQRES 13 B 666 LYS VAL ILE VAL THR SER LYS HIS ASN ASN ASP THR GLN
SEQRES 14 B 666 HIS ILE TRP GLU SER ASP SER ASN GLU PHE SER VAL ILE
SEQRES 15 B 666 ALA ASP PRO ARG GLY ASN THR LEU GLY ARG GLY THR THR
SEQRES 16 B 666 ILE THR LEU VAL LEU LYS GLU GLU ALA SER ASP TYR LEU
SEQRES 17 B 666 GLU LEU ASP THR ILE LYS ASN LEU VAL LYS LYS TYR SER
SEQRES 18 B 666 GLN PHE ILE ASN PHE PRO ILE TYR VAL TRP SER SER LYS
SEQRES 19 B 666 THR GLY GLY GLY GLY LYS THR VAL TRP ASP TRP GLU LEU
SEQRES 20 B 666 MET ASN ASP ILE LYS PRO ILE TRP GLN ARG PRO SER LYS
SEQRES 21 B 666 GLU VAL GLU ASP ASP GLU TYR LYS ALA PHE TYR LYS SER
SEQRES 22 B 666 PHE SER LYS GLU SER ASP ASP PRO MET ALA TYR ILE HIS
SEQRES 23 B 666 PHE THR ALA GLU GLY GLU VAL THR PHE LYS SER ILE LEU
SEQRES 24 B 666 PHE VAL PRO THR SER ALA PRO ARG GLY LEU PHE ASP GLU
SEQRES 25 B 666 TYR GLY SER LYS LYS SER ASP TYR ILE LYS LEU TYR VAL
SEQRES 26 B 666 ARG ARG VAL PHE ILE THR ASP ASP PHE HIS ASP MET MET
SEQRES 27 B 666 PRO LYS TYR LEU ASN PHE VAL LYS GLY VAL VAL ASP SER
SEQRES 28 B 666 ASP ASP LEU PRO LEU ASN VAL SER ARG GLU THR LEU GLN
SEQRES 29 B 666 GLN HIS LYS LEU LEU LYS VAL ILE ARG LYS LYS LEU VAL
SEQRES 30 B 666 ARG LYS THR LEU ASP MET ILE LYS LYS ILE ALA ASP GLU
SEQRES 31 B 666 LYS TYR ASN ASP THR PHE TRP LYS GLU PHE GLY THR ASN
SEQRES 32 B 666 ILE LYS LEU GLY VAL ILE GLU ASP HIS SER ASN ARG THR
SEQRES 33 B 666 ARG LEU ALA LYS LEU LEU ARG PHE GLN SER SER HIS HIS
SEQRES 34 B 666 PRO SER ASP ILE THR SER LEU ASP GLN TYR VAL GLU ARG
SEQRES 35 B 666 MET LYS GLU LYS GLN ASP LYS ILE TYR PHE MET ALA GLY
SEQRES 36 B 666 SER SER ARG LYS GLU ALA GLU SER SER PRO PHE VAL GLU
SEQRES 37 B 666 ARG LEU LEU LYS LYS GLY TYR GLU VAL ILE TYR LEU THR
SEQRES 38 B 666 GLU PRO VAL ASP GLU TYR CYS ILE GLN ALA LEU PRO GLU
SEQRES 39 B 666 PHE ASP GLY LYS ARG PHE GLN ASN VAL ALA LYS GLU GLY
SEQRES 40 B 666 VAL LYS PHE ASP GLU SER GLU LYS THR LYS GLU SER ARG
SEQRES 41 B 666 GLU ALA ILE GLU LYS GLU PHE GLU PRO LEU LEU ASN TRP
SEQRES 42 B 666 MET LYS ASP LYS ALA LEU LYS ASP LYS ILE GLU LYS ALA
SEQRES 43 B 666 VAL VAL SER GLN ARG LEU THR GLU SER PRO CYS ALA LEU
SEQRES 44 B 666 VAL ALA SER GLN TYR GLY TRP SER GLY ASN MET GLU ARG
SEQRES 45 B 666 ILE MET LYS ALA GLN ALA TYR GLN THR GLY LYS ASP ILE
SEQRES 46 B 666 SER THR ASN TYR TYR ALA SER GLN LYS LYS THR PHE GLU
SEQRES 47 B 666 ILE ASN PRO ARG HIS PRO LEU ILE LYS ASP MET LEU ARG
SEQRES 48 B 666 ARG VAL LYS GLU ASP GLU ASP ASP LYS THR VAL SER ASP
SEQRES 49 B 666 LEU ALA VAL VAL LEU PHE GLU THR ALA THR LEU ARG SER
SEQRES 50 B 666 GLY TYR LEU LEU PRO ASP THR LYS ALA TYR GLY ASP ARG
SEQRES 51 B 666 ILE GLU ARG MET LEU ARG LEU SER LEU ASN ILE ASP PRO
SEQRES 52 B 666 ASP ALA LYS
HET MG A 302 1
HET MG A 303 1
HET ANP A 755 31
HET MG B 301 1
HET MG B 304 1
HET MG B 305 1
HET ANP B 755 31
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 3 MG 5(MG 2+)
FORMUL 5 ANP 2(C10 H17 N6 O12 P3)
FORMUL 10 HOH *236(H2 O)
HELIX 1 1 ILE A 99 SER A 119 1 21
HELIX 2 2 THR A 155 LEU A 163 1 9
HELIX 3 3 PHE A 199 LEU A 204 5 6
HELIX 4 4 ASP A 262 SER A 272 1 11
HELIX 5 5 GLU A 351 PHE A 362 1 12
HELIX 6 6 PRO A 427 ASN A 431 5 5
HELIX 7 7 SER A 447 GLN A 453 1 7
HELIX 8 8 HIS A 454 ILE A 475 1 22
HELIX 9 9 ALA A 476 THR A 483 1 8
HELIX 10 10 THR A 483 ASP A 499 1 17
HELIX 11 11 ASN A 502 LYS A 508 1 7
HELIX 12 12 SER A 523 MET A 531 1 9
HELIX 13 13 SER A 545 SER A 551 1 7
HELIX 14 14 SER A 552 PHE A 554 5 3
HELIX 15 15 VAL A 555 LYS A 561 1 7
HELIX 16 16 PRO A 571 ALA A 579 1 9
HELIX 17 17 SER A 601 PHE A 615 1 15
HELIX 18 18 PHE A 615 LYS A 625 1 11
HELIX 19 19 SER A 655 THR A 669 1 15
HELIX 20 20 HIS A 691 ASP A 704 1 14
HELIX 21 21 ASP A 707 GLY A 726 1 20
HELIX 22 22 ASP A 731 LEU A 745 1 15
HELIX 23 23 ILE B 99 SER B 119 1 21
HELIX 24 24 THR B 155 LEU B 163 1 9
HELIX 25 25 GLY B 198 LEU B 204 5 7
HELIX 26 26 SER B 256 LEU B 259 5 4
HELIX 27 27 GLU B 260 TYR B 271 1 12
HELIX 28 28 PRO B 341 ARG B 345 5 5
HELIX 29 29 GLU B 351 LYS B 364 1 14
HELIX 30 30 PRO B 427 ASN B 431 5 5
HELIX 31 31 SER B 447 GLN B 453 1 7
HELIX 32 32 HIS B 454 ILE B 475 1 22
HELIX 33 33 ALA B 476 THR B 483 1 8
HELIX 34 34 THR B 483 ASP B 499 1 17
HELIX 35 35 ASN B 502 LYS B 508 1 7
HELIX 36 36 LEU B 524 MET B 531 1 8
HELIX 37 37 SER B 545 SER B 551 1 7
HELIX 38 38 SER B 552 PHE B 554 5 3
HELIX 39 39 VAL B 555 LYS B 561 1 7
HELIX 40 40 GLU B 570 ALA B 579 1 10
HELIX 41 41 SER B 601 LYS B 625 1 25
HELIX 42 42 SER B 655 TYR B 667 1 13
HELIX 43 43 HIS B 691 LYS B 702 1 12
HELIX 44 44 ASP B 707 SER B 725 1 19
HELIX 45 45 ASP B 731 ILE B 749 1 19
SHEET 1 A 8 SER A 231 ALA A 234 0
SHEET 2 A 8 HIS A 221 SER A 225 -1 N ILE A 222 O ILE A 233
SHEET 3 A 8 ALA A 206 LYS A 214 -1 N SER A 213 O HIS A 221
SHEET 4 A 8 GLY A 244 LEU A 251 -1 O THR A 246 N THR A 212
SHEET 5 A 8 LEU A 144 ASP A 149 -1 N VAL A 147 O ILE A 247
SHEET 6 A 8 VAL A 134 ASP A 139 -1 N LYS A 135 O THR A 148
SHEET 7 A 8 ILE A 279 SER A 283 1 O TYR A 280 N VAL A 134
SHEET 8 A 8 ASP A 332 LEU A 335 -1 O ASP A 332 N SER A 283
SHEET 1 B 5 ALA A 371 ALA A 377 0
SHEET 2 B 5 PHE A 383 VAL A 389 -1 O PHE A 383 N ALA A 377
SHEET 3 B 5 LYS A 434 SER A 439 -1 O LYS A 434 N PHE A 388
SHEET 4 B 5 ILE A 409 VAL A 413 1 N TYR A 412 O VAL A 437
SHEET 5 B 5 VAL A 416 THR A 419 -1 O THR A 419 N LEU A 411
SHEET 1 C 5 ILE A 521 THR A 522 0
SHEET 2 C 5 PHE A 512 SER A 514 -1 N PHE A 512 O THR A 522
SHEET 3 C 5 ILE A 566 LEU A 568 -1 O TYR A 567 N GLN A 513
SHEET 4 C 5 LYS A 537 ALA A 542 1 N TYR A 539 O ILE A 566
SHEET 5 C 5 ARG A 587 ASN A 590 1 O ARG A 587 N ILE A 538
SHEET 1 D 3 ILE A 631 VAL A 636 0
SHEET 2 D 3 LYS A 683 ILE A 687 1 O LYS A 683 N GLU A 632
SHEET 3 D 3 CYS A 645 VAL A 648 -1 N VAL A 648 O THR A 684
SHEET 1 E 8 PHE B 230 ALA B 234 0
SHEET 2 E 8 HIS B 221 SER B 225 -1 N ILE B 222 O ILE B 233
SHEET 3 E 8 ALA B 206 LYS B 214 -1 N VAL B 211 O TRP B 223
SHEET 4 E 8 GLY B 244 LEU B 251 -1 O THR B 248 N ILE B 210
SHEET 5 E 8 LEU B 144 ASP B 149 -1 N ASP B 149 O THR B 245
SHEET 6 E 8 VAL B 134 ASP B 139 -1 N LYS B 135 O THR B 148
SHEET 7 E 8 ILE B 279 SER B 284 1 O TYR B 280 N VAL B 134
SHEET 8 E 8 TRP B 331 LEU B 335 -1 O ASP B 332 N SER B 283
SHEET 1 F 5 ALA B 371 ALA B 377 0
SHEET 2 F 5 PHE B 383 VAL B 389 -1 O VAL B 389 N ALA B 371
SHEET 3 F 5 LYS B 434 SER B 439 -1 O LYS B 434 N PHE B 388
SHEET 4 F 5 ILE B 409 VAL B 413 1 N TYR B 412 O VAL B 437
SHEET 5 F 5 VAL B 416 THR B 419 -1 O THR B 419 N LEU B 411
SHEET 1 G 5 ILE B 521 SER B 523 0
SHEET 2 G 5 ARG B 511 SER B 514 -1 N PHE B 512 O THR B 522
SHEET 3 G 5 VAL B 565 LEU B 568 -1 O TYR B 567 N GLN B 513
SHEET 4 G 5 LYS B 537 ALA B 542 1 N MET B 541 O LEU B 568
SHEET 5 G 5 ARG B 587 ASN B 590 1 O GLN B 589 N ILE B 538
SHEET 1 H 3 LYS B 633 VAL B 636 0
SHEET 2 H 3 THR B 684 ILE B 687 1 O PHE B 685 N LYS B 633
SHEET 3 H 3 CYS B 645 VAL B 648 -1 N VAL B 648 O THR B 684
LINK OD1 ASN A 107 MG MG A 302 1555 1555 2.22
LINK MG MG A 302 O1G ANP A 755 1555 1555 2.39
LINK MG MG A 302 O1A ANP A 755 1555 1555 2.17
LINK MG MG A 302 O2B ANP A 755 1555 1555 1.78
LINK OD1 ASN B 107 MG MG B 301 1555 1555 2.30
LINK MG MG B 301 O1G ANP B 755 1555 1555 2.37
CRYST1 99.330 109.260 148.887 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009152 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006717 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
